MolNFT v1 · #13783 · protein

Crystal structure of mthk at 3.3 a

1LNQ · Potassium channel related protein: “Crystal structure of mthk at 3.3 a”. X-ray diffraction, 1 ligand (CA), 20 pockets (best druggability 0.82). MolNFT v1 #13783 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LNQ
Type: protein
Length: 2,408 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium channel related protein
UniProt: O27564
Ligands: CA
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Potassium channel related protein	protein	301	37% helix, 17% strand	O27564

Ligands and binding sites

CA · Calcium ion · metal · 8 copies · chains A, G, B, F, C, E, D, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1151	0.82	0.83	152	empty
2	722	0.81	0.85	110	empty
3	169	0.72	0.90	37	empty
4	144	0.72	0.92	35	empty
5	217	0.72	0.88	37	empty

Interfaces

20 interfaces between chains.

A–G · 3762 Å² buried · 43 hydrogen bonds · protein-protein
C–E · 3758 Å² buried · 45 hydrogen bonds · protein-protein
B–F · 3741 Å² buried · 40 hydrogen bonds · protein-protein
D–H · 3729 Å² buried · 40 hydrogen bonds · protein-protein
A–H · 824 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1LNQ · Crystal structure of mthk at 3.3 a · the same entry in another collection · chain F against F, TM-score 1.00
O27564 · AlphaFold monomer V2.0 prediction for calcium-gated potassium channel mthk (O27564) · a predicted model of the same protein · chain A against A, TM-score 0.80

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O27564
Elsewhere: RCSB PDB 1LNQ · PDBe 1LNQ · UniProt O27564

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